Structure of PDB 1ib1 Chain F

Receptor sequence
>1ib1F (length=179) Species: 9940 (Ovis aries) [Search protein sequence]
SGIPGSPGRQRRHTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNL
DEVQHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLALHRPRGH
SAHLHALAVHRSFRQQGKGSVLLWRYLHHVGAQPAVRRAVLMCEDALVPF
YQRFGFHPAGPCAIVVGSLTFTEMHCSLR
3D structure
PDB1ib1 Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.
ChainF
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S97 L111 H122 L124 Y168
Catalytic site (residue number reindexed from 1) S80 L94 H105 L107 Y151
Enzyme Commision number 2.3.1.87: aralkylamine N-acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 COT F F56 C63 P64 A123 L124 A125 V126 R131 Q132 G134 G136 S137 M159 E161 A163 L164 F167 Y168 R170 F188 F39 C46 P47 A106 L107 A108 V109 R114 Q115 G117 G119 S120 M142 E144 A146 L147 F150 Y151 R153 F171
Gene Ontology
Molecular Function
GO:0004059 aralkylamine N-acetyltransferase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006474 N-terminal protein amino acid acetylation
GO:0007623 circadian rhythm
GO:0009416 response to light stimulus
GO:0030187 melatonin biosynthetic process
GO:0048511 rhythmic process
GO:0071320 cellular response to cAMP
Cellular Component
GO:0005737 cytoplasm
GO:0048471 perinuclear region of cytoplasm

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Cellular Component
External links
PDB RCSB:1ib1, PDBe:1ib1, PDBj:1ib1
PDBsum1ib1
PubMed11336675
UniProtQ29495|SNAT_SHEEP Serotonin N-acetyltransferase (Gene Name=AANAT)

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